Peptidoglycolipid nature of the superficial cell wall sheath of smooth-colony-forming mycobacteria

Publisher Website
Google Scholar
Abstract
The most superficial cell wall layer present in smooth-colony-forming mycobacteria was isolated from serovar 20 of the Mycobacterium avium-M. intracellulare-M. scrofulaceum (MAIS) serocomplex and examined chemically and by EM. Most (70-80%) of the fibrillar material consisted of an array of serologically active, acetylated C-mycosidic peptidoglycolipids but in which the location of acetyl groups and the arrangement of monosaccharides were not defined. Apparently, all serovars within the MAIS complex are characterized by structurally related superficies in which the monoglycosyllipopeptide portion is invariable but the oligosaccharide attachment is peculiar to each serovar. These unique inert structures may be an important factor in shielding the pathogen within phagolysosomes from lysosomal enzymes.